4PHC

Crystal Structure of a human cytosolic histidyl-tRNA synthetase, histidine-bound

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003723	molecular_function	RNA binding
A	0004812	molecular_function	aminoacyl-tRNA ligase activity
A	0004821	molecular_function	histidine-tRNA ligase activity
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006412	biological_process	translation
A	0006418	biological_process	tRNA aminoacylation for protein translation
A	0006427	biological_process	histidyl-tRNA aminoacylation
A	0016874	molecular_function	ligase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
B	0000166	molecular_function	nucleotide binding
B	0003723	molecular_function	RNA binding
B	0004812	molecular_function	aminoacyl-tRNA ligase activity
B	0004821	molecular_function	histidine-tRNA ligase activity
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006412	biological_process	translation
B	0006418	biological_process	tRNA aminoacylation for protein translation
B	0006427	biological_process	histidyl-tRNA aminoacylation
B	0016874	molecular_function	ligase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
C	0000166	molecular_function	nucleotide binding
C	0003723	molecular_function	RNA binding
C	0004812	molecular_function	aminoacyl-tRNA ligase activity
C	0004821	molecular_function	histidine-tRNA ligase activity
C	0005524	molecular_function	ATP binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006412	biological_process	translation
C	0006418	biological_process	tRNA aminoacylation for protein translation
C	0006427	biological_process	histidyl-tRNA aminoacylation
C	0016874	molecular_function	ligase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
D	0000166	molecular_function	nucleotide binding
D	0003723	molecular_function	RNA binding
D	0004812	molecular_function	aminoacyl-tRNA ligase activity
D	0004821	molecular_function	histidine-tRNA ligase activity
D	0005524	molecular_function	ATP binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006412	biological_process	translation
D	0006418	biological_process	tRNA aminoacylation for protein translation
D	0006427	biological_process	histidyl-tRNA aminoacylation
D	0016874	molecular_function	ligase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue HIS A 1001

Chain	Residue
A	ASP130
A	TYR331
A	GLY360
A	TYR363
A	GLY381
A	LEU382
A	SER383
A	HOH1113
A	THR132
A	ARG157
A	GLN173
A	ASP175
A	ASP177
A	ARG326
A	LEU328
A	TYR330

---

site_id	AC2
Number of Residues	2
Details	binding site for residue GOL A 1002

Chain	Residue
A	ASN146
B	TYR454

---

site_id	AC3
Number of Residues	14
Details	binding site for residue HIS B 1001

Chain	Residue
B	ASP130
B	THR132
B	ARG157
B	GLN173
B	ASP175
B	ASP177
B	ARG326
B	TYR330
B	TYR331
B	GLY360
B	TYR363
B	GLY381
B	LEU382
B	HOH1116

---

site_id	AC4
Number of Residues	2
Details	binding site for residue GOL B 1002

Chain	Residue
A	TYR454
B	ASN146

---

site_id	AC5
Number of Residues	13
Details	binding site for residue HIS C 1001

Chain	Residue
C	ASP130
C	THR132
C	ARG157
C	GLN173
C	ASP175
C	ASP177
C	ARG326
C	LEU328
C	TYR330
C	TYR331
C	TYR363
C	GLY381
C	LEU382

---

site_id	AC6
Number of Residues	2
Details	binding site for residue GOL C 1002

Chain	Residue
C	ASN146
D	TYR454

---

site_id	AC7
Number of Residues	3
Details	binding site for residue GOL C 1003

Chain	Residue
C	TYR454
D	GLU90
D	ASN146

---

site_id	AC8
Number of Residues	14
Details	binding site for residue HIS D 1001

Chain	Residue
D	ASP130
D	THR132
D	ARG157
D	GLN173
D	ASP175
D	ASP177
D	ARG326
D	TYR330
D	TYR331
D	GLY360
D	GLY381
D	LEU382
D	SER383
D	HOH1109

---

Functional Information from PROSITE/UniProt

site_id	PS00762
Number of Residues	29
Details	WHEP_TRS_1 WHEP-TRS domain signature. QGErVRglKqqKAsaelIEeeVakLlklK

Chain	Residue	Details
A	GLN14-LYS42

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25151410","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4PHC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99KK9","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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